The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier.

@article{Bock2002TheUH,
  title={The unorthodox histidine kinases BvgS and EvgS are responsive to the oxidation status of a quinone electron carrier.},
  author={Andreas Bock and Roy Gross},
  journal={European journal of biochemistry},
  year={2002},
  volume={269 14},
  pages={3479-84}
}
The purified soluble forms of the histidine kinases BvgS and EvgS of Bordetella pertussis and Escherichia coli, respectively, are shown to be responsive to oxidized ubiquinone-0 (Q-0) in vitro. The oxidized ubiquinone is a strong inhibitor of kinase activity of both enzymes with half maximal inhibition occurring at 11 microm (BvgS) and 4 microm (EvgS). Reduced Q-0 has no effect on the histidine kinases. Kinase activity can reversibly be switched off and on by changing the oxidation status of… CONTINUE READING
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